PMID: 6268171Jul 24, 1981

Tonin, an esteroprotease from rat submaxillary glands

Biochimica Et Biophysica Acta
G Thibault, J Genest

Abstract

Tonin is an enzyme found in the rat submaxillary glands which liberates angiotensin II from angiotensinogen, the Skeggs tetradecapeptide renin substrate, and angiotensin I. Tonin hydrolyzes benzoyl-arginine ethyl ester, benzoyl-arginine methyl ester, tosyl-arginine methyl ester, benzoyl-arginine p-nitroanilide and other small synthetic substrates at an optimum ph of 9.0. Tonin shows, however, a great specificity with respect to angiotensin I. Tonin is inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride at high concentrations (greater than 10(-2) M) and by soybean trypsin inhibitor and aprotinin. Tonin is thus an esteroprotease of the class of the serine protease with trypsin- and chymotrypsin-like activity. Tonin belongs to the same family of enzyme as glandular kallikrein and the gamma subunit of the nerve growth factor.

References

Jan 1, 1981·Hypertension·M IkedaJ Genest

Citations

Jun 1, 1991·Journal of Molecular Evolution·D R WinesR J MacDonald
May 1, 1993·The International Journal of Biochemistry·B L SlomianyA Slomiany
Jul 1, 1996·General Pharmacology·B L SlomianyA Slomiany
Oct 1, 1992·Experimental Eye Research·T OkamuraN Toda
Nov 1, 1982·Analytical Biochemistry·E S Cheng, B J Morris
Oct 29, 1982·Biochemical and Biophysical Research Communications·J L PesqueroA C Paiva
Jan 1, 1986·Archives of Oral Biology·K IkenoI Ishiguro
Mar 1, 1984·Hypertension·M Ikeda, K Arakawa
Jan 1, 1988·Hypertension·M IkedaK Arakawa
Feb 1, 1988·European Journal of Biochemistry·N GutmanF Gauthier
May 1, 1996·Preparative Biochemistry & Biotechnology·G S Bedi

Related Concepts

Angiotensin I
Angiotensin II, Val(5)-
Angiotensin-Converting Enzyme Inhibitors
Renin Substrate Tetradecapeptide
Metazoa
Peptidyl-Dipeptidase A
Submandibular Gland
Substrate Specificity
Macromolecular Compounds
Rats, Laboratory

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